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Conserved domains on  [gi|380420360|ref|NP_001244075|]
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protein flightless-1 homolog [Danio rerio]

Protein Classification

protein flightless-1 homolog( domain architecture ID 13320407)

protein flightless-1 homolog may play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 491-603 2.97e-56

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200446  Cd Length: 113  Bit Score: 190.13  E-value: 2.97e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  491 LEDVGQIPGVSVWQIENFIPIQVDEAFHGKFYEADCYIILKTFLDENGALNWQIFYWIGQDATLDKKAGAAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 380420360  571 LGAECRTIREEMGDESEEFTVVFDHEISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1153-1252 2.34e-45

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 158.61  E-value: 2.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1153 YARLFRCSNEKGYFaVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTENPRKL 1232
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 380420360 1233 RLVRKGNEPHCFTRCFHAWS 1252
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
102-373 1.50e-42

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 161.25  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  102 QLDDLSVLDLSHNQLTEIPRDLENSRNMLVLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLIL 181
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  182 NNNPLMHAQLRQLPvmvSLQTLHLRNTQrtqnnmptSLEGLSNLTDVDLSCNDLTRVPECLYSLVNLKRLNLSSNQISEL 261
Cdd:COG4886    83 SLLLLGLTDLGDLT---NLTELDLSGNE--------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  262 SLCIDQWTKLETLNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDFdgLPSGVGKLSNLVEFMAANNNLELVPEGLCRCGK 341
Cdd:COG4886   152 PEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQLTDLPEPLANLTN 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 380420360  342 LKKLVLNKNRLVTLPEaIHFLTELEVLDVREN 373
Cdd:COG4886   230 LETLDLSNNQLTDLPE-LGNLTNLEELDLSNN 260
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1043-1142 3.87e-35

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200444  Cd Length: 92  Bit Score: 128.89  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1043 QPSLYHIRTNGSaLCTRTIQIATDSSNLNSEFCFILKVPFestdnqgIVYTWVGRAADPDEAKLAEEIMNTMFDDtYSKQ 1122
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKPK-ASLQ 72

                          90       100
                  ....*....|....*....|
gi 380420360 1123 VINEGEEPENFFWVGIGSQK 1142
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 722-836 6.61e-31

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200448  Cd Length: 98  Bit Score: 116.97  E-value: 6.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  722 PIRPKLYKVGLGLGYLELPQINYKLsvehkdklkldvvpelrLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 380420360  802 LGQEVCGMLHRPKHAVVIRNLEGTECQVFKSKFKN 836
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 617-705 1.48e-25

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200436  Cd Length: 88  Bit Score: 101.68  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  617 PTRLYRVYGKKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKnERKSKAEITTLMQNQ 696
Cdd:cd11280     1 PPRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQ 79


                  ....*....
gi 380420360  697 EPPEFWEVL 705
Cdd:cd11280    80 EPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 931-1024 5.33e-19

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.80  E-value: 5.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  931 DCYVFLCRYWVPVEYEDDKEKGKEKGEEGddeekQPEEDFQCVVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVR 1010
Cdd:cd11280     1 PPRLYRVRGSKAIEIEEVPLASSSLDSDD-----VFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 380420360 1011 MTQQQENLKFLSHF 1024
Cdd:cd11280    75 IRQGQEPREFWSLF 88
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 10-163 2.22e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 54.28  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   10 IRGVDLSGNDFKGGNFP--EHVKSMTSLRWLKLNR------------TGLCYLPEELASLQkLEHLSVSHNSLTTLHGEL 75
Cdd:cd00116    83 LQELDLSDNALGPDGCGvlESLLRSSSLQELKLNNnglgdrglrllaKGLKDLPPALEKLV-LGRNRLEGASCEALAKAL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   76 SSLPNLRAVVARANNLKNSGVP---DDIFQLDDLSVLDLSHNQLT--------EIPRDLensRNMLVLNLSHNSIDNIP- 143
Cdd:cd00116   162 RANRDLKELNLANNGIGDAGIRalaEGLKANCNLEVLDLNNNGLTdegasalaETLASL---KSLEVLNLGDNNLTDAGa 238

                         170       180
                  ....*....|....*....|....
gi 380420360  144 ----NQLFINLTDLLYLDLSDNNL 163
Cdd:cd00116   239 aalaSALLSPNISLLTLSLSCNDI 262
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 491-603 2.97e-56

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 190.13  E-value: 2.97e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  491 LEDVGQIPGVSVWQIENFIPIQVDEAFHGKFYEADCYIILKTFLDENGALNWQIFYWIGQDATLDKKAGAAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 380420360  571 LGAECRTIREEMGDESEEFTVVFDHEISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1153-1252 2.34e-45

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 158.61  E-value: 2.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1153 YARLFRCSNEKGYFaVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTENPRKL 1232
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 380420360 1233 RLVRKGNEPHCFTRCFHAWS 1252
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
102-373 1.50e-42

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 161.25  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  102 QLDDLSVLDLSHNQLTEIPRDLENSRNMLVLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLIL 181
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  182 NNNPLMHAQLRQLPvmvSLQTLHLRNTQrtqnnmptSLEGLSNLTDVDLSCNDLTRVPECLYSLVNLKRLNLSSNQISEL 261
Cdd:COG4886    83 SLLLLGLTDLGDLT---NLTELDLSGNE--------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  262 SLCIDQWTKLETLNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDFdgLPSGVGKLSNLVEFMAANNNLELVPEGLCRCGK 341
Cdd:COG4886   152 PEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQLTDLPEPLANLTN 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 380420360  342 LKKLVLNKNRLVTLPEaIHFLTELEVLDVREN 373
Cdd:COG4886   230 LETLDLSNNQLTDLPE-LGNLTNLEELDLSNN 260
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1043-1142 3.87e-35

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 128.89  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1043 QPSLYHIRTNGSaLCTRTIQIATDSSNLNSEFCFILKVPFestdnqgIVYTWVGRAADPDEAKLAEEIMNTMFDDtYSKQ 1122
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKPK-ASLQ 72

                          90       100
                  ....*....|....*....|
gi 380420360 1123 VINEGEEPENFFWVGIGSQK 1142
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 722-836 6.61e-31

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 116.97  E-value: 6.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  722 PIRPKLYKVGLGLGYLELPQINYKLsvehkdklkldvvpelrLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 380420360  802 LGQEVCGMLHRPKHAVVIRNLEGTECQVFKSKFKN 836
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 5-417 7.47e-30

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 128.81  E-value: 7.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    5 GVLPFIRGVDLSGNDFKGgNFPEHVKSMTSLRWLKLNRTGLC-YLPEELASLQKLEHLSVSHNSLT-TLHGELSSLPNLR 82
Cdd:PLN00113  137 GSIPNLETLDLSNNMLSG-EIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLK 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   83 AVVARANNLkNSGVPDDIFQLDDLSVLDLSHNQLT-EIPRDLENSRNMLVLNLSHNSI-DNIPNQLFiNLTDLLYLDLSD 160
Cdd:PLN00113  216 WIYLGYNNL-SGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSD 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  161 NNLD-SLPPQMRRLVHLQTLILNNNPLMHAQLRQLPVMVSLQTLHLRnTQRTQNNMPTSLEGLSNLTDVDLSCNDLT-RV 238
Cdd:PLN00113  294 NSLSgEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLW-SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEI 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  239 PECLYSLVNLKRLNLSSNQIS-----ELSLC----------------------------------------ID--QW--T 269
Cdd:PLN00113  373 PEGLCSSGNLFKLILFSNSLEgeipkSLGACrslrrvrlqdnsfsgelpseftklplvyfldisnnnlqgrINsrKWdmP 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  270 KLETLNLSRNQLT-SLPSAIcKLSKLKKLYVNSNKIDfDGLPSGVGKLSNLVEFMAANNNLE-LVPEGLCRCGKLKKLVL 347
Cdd:PLN00113  453 SLQMLSLARNKFFgGLPDSF-GSKRLENLDLSRNQFS-GAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDL 530

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380420360  348 NKNRLV-TLPEAIHFLTELEVLDVRENPNLVMPPKPVDRTAEWYNIDFS---LQNQLRLAGASPATVAAAGGGN 417
Cdd:PLN00113  531 SHNQLSgQIPASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNIShnhLHGSLPSTGAFLAINASAVAGN 604
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 617-705 1.48e-25

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 101.68  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  617 PTRLYRVYGKKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKnERKSKAEITTLMQNQ 696
Cdd:cd11280     1 PPRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQ 79


                  ....*....
gi 380420360  697 EPPEFWEVL 705
Cdd:cd11280    80 EPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-707 1.79e-24

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.52  E-value: 1.79e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    619 RLYRVYGKKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKNERKSKAEITTLMQNQEP 698
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 380420360    699 PEFWEVLGG 707
Cdd:smart00262   81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1158-1251 1.34e-23

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.82  E-value: 1.34e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   1158 RCSNEKGYFAVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTenprKLRLVRK 1237
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPV----QVRVVDE 76

                            90
                    ....*....|....
gi 380420360   1238 GNEPHCFTRCFHAW 1251
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 931-1024 5.33e-19

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.80  E-value: 5.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  931 DCYVFLCRYWVPVEYEDDKEKGKEKGEEGddeekQPEEDFQCVVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVR 1010
Cdd:cd11280     1 PPRLYRVRGSKAIEIEEVPLASSSLDSDD-----VFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 380420360 1011 MTQQQENLKFLSHF 1024
Cdd:cd11280    75 IRQGQEPREFWSLF 88
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-308 7.14e-19

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 86.76  E-value: 7.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  103 LDDLSVLDLSHNQLTEIPrDLENSRNMLVLNLSHNSIDNIPNqlFINLTDLLYLDLSDNNLDSLPPqMRRLVHLQTLILN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  183 NNPLMH-AQLRQLPvmvSLQTLHLRNtQRTQNNM-----PTSLEGLSN-LTDVDLSCNDLTRVpECLYSLVNLKRLNLSS 255
Cdd:cd21340    77 GNRISVvEGLENLT---NLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 380420360  256 NQIS---ELSLCIDQWTKLETLNLSRNqltslPsaICKLSKLK-KLYVNSNKID-FDG 308
Cdd:cd21340   152 NQISdleELLDLLSSWPSLRELDLTGN-----P--VCKKPKYRdKIILASKSLEvLDG 202
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 758-837 8.23e-18

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 79.64  E-value: 8.23e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    758 VVPELRLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALKLGQEVCGMLHrPKHAVVIRNLEGTECQVFKSKFKNW 837
Cdd:smart00262   12 RVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 501-593 9.39e-17

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 76.56  E-value: 9.39e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    501 SVWQIENFIPIQVDE--AFHGKFYEADCYIILKTfldengalnWQIFYWIGQDATLDKKAGAAIHAVNLRNYLGAECRTI 578
Cdd:smart00262    1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                            90
                    ....*....|....*.
gi 380420360    579 RE-EMGDESEEFTVVF 593
Cdd:smart00262   72 RVvDEGKEPPEFWSLF 87
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1047-1139 1.09e-14

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 70.78  E-value: 1.09e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   1047 YHIRTNGSaLCTRTIQIATDSSNLNSEFCFILkvpfestDNQGIVYTWVGRAADPDE----AKLAEEIMNTMFDDTYSKQ 1122
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEkkkaAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 380420360   1123 VINEGEEPENFFWVGIG 1139
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
627-702 1.58e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.64  E-value: 1.58e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380420360   627 KNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKNERKSKAEITTLMQNQEPPEFW 702
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
507-589 6.45e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 65.02  E-value: 6.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   507 NFIPIQVDEAFHGKFYEADCYIILKTFldengalnwQIFYWIGQDATLDKKAGAAIHAVNLR-NYLGAECRTIREEMGDE 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....
gi 380420360   586 SEEF 589
Cdd:pfam00626   72 PARF 75
LRR_8 pfam13855
Leucine rich repeat;
127-186 3.87e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 3.87e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380420360   127 RNMLVLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQM-RRLVHLQTLILNNNPL 186
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
755-831 8.36e-08

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 50.77  E-value: 8.36e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380420360   755 KLDVVPELRLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALKLGQEVcGMLHRPKHAVVIRNLEGTECQVFK 831
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 10-163 2.22e-07

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 54.28  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   10 IRGVDLSGNDFKGGNFP--EHVKSMTSLRWLKLNR------------TGLCYLPEELASLQkLEHLSVSHNSLTTLHGEL 75
Cdd:cd00116    83 LQELDLSDNALGPDGCGvlESLLRSSSLQELKLNNnglgdrglrllaKGLKDLPPALEKLV-LGRNRLEGASCEALAKAL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   76 SSLPNLRAVVARANNLKNSGVP---DDIFQLDDLSVLDLSHNQLT--------EIPRDLensRNMLVLNLSHNSIDNIP- 143
Cdd:cd00116   162 RANRDLKELNLANNGIGDAGIRalaEGLKANCNLEVLDLNNNGLTdegasalaETLASL---KSLEVLNLGDNNLTDAGa 238

                         170       180
                  ....*....|....*....|....
gi 380420360  144 ----NQLFINLTDLLYLDLSDNNL 163
Cdd:cd00116   239 aalaSALLSPNISLLTLSLSCNDI 262
Gelsolin pfam00626
Gelsolin repeat;
1166-1227 4.87e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.46  E-value: 4.87e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380420360  1166 FAVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTE 1227
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPE 62
Gelsolin pfam00626
Gelsolin repeat;
1066-1133 1.50e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 41.52  E-value: 1.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380420360  1066 DSSNLNSEFCFILkvpfestDNQGIVYTWVGRAADPDE----AKLAEEIMNTMFDDTYSKQVINEGEEPENF 1133
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
LRR_8 pfam13855
Leucine rich repeat;
33-91 1.97e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.59  E-value: 1.97e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380420360    33 TSLRWLKLNRTGLCYLPEE-LASLQKLEHLSVSHNSLTTLH-GELSSLPNLRAVVARANNL 91
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 33-139 4.85e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.95  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   33 TSLRW----LKLNRTGL-CYLPEELASLQKLEHLSVSHNSLttlHGElsslpnlravvarannlknsgVPDDIFQLDDLS 107
Cdd:PLN03150  414 TKGKWfidgLGLDNQGLrGFIPNDISKLRHLQSINLSGNSI---RGN---------------------IPPSLGSITSLE 469

                          90       100       110
                  ....*....|....*....|....*....|...
gi 380420360  108 VLDLSHNQLT-EIPRDLENSRNMLVLNLSHNSI 139
Cdd:PLN03150  470 VLDLSYNSFNgSIPESLGQLTSLRILNLNGNSL 502
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 491-603 2.97e-56

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 190.13  E-value: 2.97e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  491 LEDVGQIPGVSVWQIENFIPIQVDEAFHGKFYEADCYIILKTFLDENGALNWQIFYWIGQDATLDKKAGAAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 380420360  571 LGAECRTIREEMGDESEEFTVVFDHEISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1153-1252 2.34e-45

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 158.61  E-value: 2.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1153 YARLFRCSNEKGYFaVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTENPRKL 1232
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 380420360 1233 RLVRKGNEPHCFTRCFHAWS 1252
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
102-373 1.50e-42

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 161.25  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  102 QLDDLSVLDLSHNQLTEIPRDLENSRNMLVLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLIL 181
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  182 NNNPLMHAQLRQLPvmvSLQTLHLRNTQrtqnnmptSLEGLSNLTDVDLSCNDLTRVPECLYSLVNLKRLNLSSNQISEL 261
Cdd:COG4886    83 SLLLLGLTDLGDLT---NLTELDLSGNE--------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  262 SLCIDQWTKLETLNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDFdgLPSGVGKLSNLVEFMAANNNLELVPEGLCRCGK 341
Cdd:COG4886   152 PEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQLTDLPEPLANLTN 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 380420360  342 LKKLVLNKNRLVTLPEaIHFLTELEVLDVREN 373
Cdd:COG4886   230 LETLDLSNNQLTDLPE-LGNLTNLEELDLSNN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
114-374 2.53e-42

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 160.87  E-value: 2.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  114 NQLTEIPRDLENSRNMLVLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLILNNNplmhaqlRQ 193
Cdd:COG4886    36 ALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  194 LPVMVSLQTLHLRNTQRTqnNMPTSLEGLSNLTDVDLSCNDLTRVPECLYSLVNLKRLNLSSNQISELSLCIDQWTKLET 273
Cdd:COG4886   109 LSNLTNLESLDLSGNQLT--DLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  274 LNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDfdGLPSGVGKLSNLVEFMAANNNLELVPEgLCRCGKLKKLVLNKNRLV 353
Cdd:COG4886   187 LDLSNNQITDLPEPLGNLTNLEELDLSGNQLT--DLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLT 263

                         250       260
                  ....*....|....*....|.
gi 380420360  354 TLPEAIHfLTELEVLDVRENP 374
Cdd:COG4886   264 DLPPLAN-LTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-355 3.14e-42

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 160.48  E-value: 3.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   38 LKLNRTGLCYLPEELASLQKLEHLSVSHNSLTTLHGELSSLPNLRAVVARANNLKNSGVPDDIFQLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  118 E---IPRDLENSRNMLVLNLSHNsidnipnQLFINLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLILNNNPLmhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  195 pvmvslqtlhlrntqrtqNNMPTSLEGLSNLTDVDLSCNDLTRVPECLYSLVNLKRLNLSSNQISELSLCIDQWTKLETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  275 NLSRNQLTSLPSAICKLSKLKKLYVNSNKIdfDGLPSgVGKLSNLVEFMAANNNLELVPEgLCRCGKLKKLVLNKNRLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEPLANLTNLETLDLSNNQL--TDLPE-LGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTD 286


                  .
gi 380420360  355 L 355
Cdd:COG4886   287 L 287
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-331 3.89e-40

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 154.32  E-value: 3.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   24 NFPEHVKSMTSLRWLKLNRTglcylpEELASLQKLEHLSVSHNSLTTLHGELSSLPNLRAVVARANNLKNsgVPDDIFQL 103
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  104 DDLSVLDLSHNQLTEIPRDLENSRNMLVLNLSHNSIDNIPNQLFiNLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLILNN 183
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  184 NplmhaQLRQLPvmvslqtlhlrntqrtqnnmptSLEGLSNLTDVDLSCNDLTRVPEcLYSLVNLKRLNLSSNQISELSL 263
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380420360  264 C-IDQWTKLETLNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDFDGLPSGVGKLSNLVEFMAANNNLEL 331
Cdd:COG4886   290 KeLELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNL 358
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1043-1142 3.87e-35

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 128.89  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1043 QPSLYHIRTNGSaLCTRTIQIATDSSNLNSEFCFILKVPFestdnqgIVYTWVGRAADPDEAKLAEEIMNTMFDDtYSKQ 1122
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKPK-ASLQ 72

                          90       100
                  ....*....|....*....|
gi 380420360 1123 VINEGEEPENFFWVGIGSQK 1142
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-263 3.93e-32

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 130.82  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    7 LPFIRGVDLSGNDFKggNFPEHVKSMTSLRWLKLNRTGLCYLPEELASLQKLEHLSVSHNSLTTLHGELSSLPNLRavva 86
Cdd:COG4886   135 LTNLKELDLSNNQLT--DLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLE---- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   87 rannlknsgvpddifqlddlsVLDLSHNQLTEIPRDLENSRNMLVLNLSHNSIDNIPNqlFINLTDLLYLDLSDNNLDSL 166
Cdd:COG4886   209 ---------------------ELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDL 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  167 PPQMrRLVHLQTLILNNNPLMHAQLRQLPVMVSLQTLHLRNTQRTQNNMPTSLEGLSNLTDVDLSCNDLTRVPECLYSLV 246
Cdd:COG4886   266 PPLA-NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSL 344

                         250
                  ....*....|....*..
gi 380420360  247 NLKRLNLSSNQISELSL 263
Cdd:COG4886   345 SLLALLTLLLLLNLLSL 361
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 722-836 6.61e-31

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 116.97  E-value: 6.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  722 PIRPKLYKVGLGLGYLELPQINYKLsvehkdklkldvvpelrLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 380420360  802 LGQEVCGMLHRPKHAVVIRNLEGTECQVFKSKFKN 836
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 5-417 7.47e-30

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 128.81  E-value: 7.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    5 GVLPFIRGVDLSGNDFKGgNFPEHVKSMTSLRWLKLNRTGLC-YLPEELASLQKLEHLSVSHNSLT-TLHGELSSLPNLR 82
Cdd:PLN00113  137 GSIPNLETLDLSNNMLSG-EIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLK 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   83 AVVARANNLkNSGVPDDIFQLDDLSVLDLSHNQLT-EIPRDLENSRNMLVLNLSHNSI-DNIPNQLFiNLTDLLYLDLSD 160
Cdd:PLN00113  216 WIYLGYNNL-SGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSD 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  161 NNLD-SLPPQMRRLVHLQTLILNNNPLMHAQLRQLPVMVSLQTLHLRnTQRTQNNMPTSLEGLSNLTDVDLSCNDLT-RV 238
Cdd:PLN00113  294 NSLSgEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLW-SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEI 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  239 PECLYSLVNLKRLNLSSNQIS-----ELSLC----------------------------------------ID--QW--T 269
Cdd:PLN00113  373 PEGLCSSGNLFKLILFSNSLEgeipkSLGACrslrrvrlqdnsfsgelpseftklplvyfldisnnnlqgrINsrKWdmP 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  270 KLETLNLSRNQLT-SLPSAIcKLSKLKKLYVNSNKIDfDGLPSGVGKLSNLVEFMAANNNLE-LVPEGLCRCGKLKKLVL 347
Cdd:PLN00113  453 SLQMLSLARNKFFgGLPDSF-GSKRLENLDLSRNQFS-GAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDL 530

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380420360  348 NKNRLV-TLPEAIHFLTELEVLDVRENPNLVMPPKPVDRTAEWYNIDFS---LQNQLRLAGASPATVAAAGGGN 417
Cdd:PLN00113  531 SHNQLSgQIPASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNIShnhLHGSLPSTGAFLAINASAVAGN 604
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 2-352 3.02e-29

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 126.50  E-value: 3.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    2 AATGVLPFIRGVDLSGNDFKGGnFPEHV-KSMTSLRWLKL---NRTGlcylPEELASLQKLEHLSVSHNSLT-TLHGELS 76
Cdd:PLN00113   87 SAIFRLPYIQTINLSNNQLSGP-IPDDIfTTSSSLRYLNLsnnNFTG----SIPRGSIPNLETLDLSNNMLSgEIPNDIG 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   77 SLPNLRaVVARANNLKNSGVPDDIFQLDDLSVLDLSHNQLT-EIPRDLENSRNMLVLNLSHNSID-NIPNQLFiNLTDLL 154
Cdd:PLN00113  162 SFSSLK-VLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIG-GLTSLN 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  155 YLDLSDNNLD-SLPPQMRRLVHLQTLILNNNPLmhaqlrqlpvmvslqtlhlrntqrtQNNMPTSLEGLSNLTDVDLSCN 233
Cdd:PLN00113  240 HLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKL-------------------------SGPIPPSIFSLQKLISLDLSDN 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  234 DLtrvpeclyslvnlkrlnlsSNQISELslcIDQWTKLETLNLSRNQLT-SLPSAICKLSKLKKLYVNSNKIDfDGLPSG 312
Cdd:PLN00113  295 SL-------------------SGEIPEL---VIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFS-GEIPKN 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 380420360  313 VGKLSNLVEFMAANNNLE-LVPEGLCRCGKLKKLVLNKNRL 352
Cdd:PLN00113  352 LGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSL 392
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 617-705 1.48e-25

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 101.68  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  617 PTRLYRVYGKKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKnERKSKAEITTLMQNQ 696
Cdd:cd11280     1 PPRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQ 79


                  ....*....
gi 380420360  697 EPPEFWEVL 705
Cdd:cd11280    80 EPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-707 1.79e-24

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.52  E-value: 1.79e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    619 RLYRVYGKKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKNERKSKAEITTLMQNQEP 698
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 380420360    699 PEFWEVLGG 707
Cdd:smart00262   81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1158-1251 1.34e-23

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.82  E-value: 1.34e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   1158 RCSNEKGYFAVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTenprKLRLVRK 1237
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPV----QVRVVDE 76

                            90
                    ....*....|....
gi 380420360   1238 GNEPHCFTRCFHAW 1251
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 23-344 3.40e-21

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 100.69  E-value: 3.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   23 GNFPEHVKSMTSLRWLKLNRTGLC-YLPEELASLQKLEHLSVSHNSLT-TLHGELSSLPNLRAVVARANNLkNSGVPDDI 100
Cdd:PLN00113  274 GPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKF-SGEIPKNL 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  101 FQLDDLSVLDLSHNQLT-EIPRDLENSRNMLVLNLSHNSIDN-IPNQL-----------------------FINLTDLLY 155
Cdd:PLN00113  353 GKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGeIPKSLgacrslrrvrlqdnsfsgelpseFTKLPLVYF 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  156 LDLSDNNLD-SLPPQMRRLVHLQTLILNNNPLmhaqLRQLPVmvSLQTLHLRNTQRTQNN----MPTSLEGLSNLTDVDL 230
Cdd:PLN00113  433 LDISNNNLQgRINSRKWDMPSLQMLSLARNKF----FGGLPD--SFGSKRLENLDLSRNQfsgaVPRKLGSLSELMQLKL 506

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  231 SCNDLT-RVPECLYSLVNLKRLNLSSNQIS-ELSLCIDQWTKLETLNLSRNQLT-SLPSAICKLSKLKKLYVNSNKidFD 307
Cdd:PLN00113  507 SENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNH--LH 584

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 380420360  308 G-LPSGVGKLSNLVEFMAANNNL--ELVPEGLCRCGKLKK 344
Cdd:PLN00113  585 GsLPSTGAFLAINASAVAGNIDLcgGDTTSGLPPCKRVRK 624
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 931-1024 5.33e-19

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.80  E-value: 5.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  931 DCYVFLCRYWVPVEYEDDKEKGKEKGEEGddeekQPEEDFQCVVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVR 1010
Cdd:cd11280     1 PPRLYRVRGSKAIEIEEVPLASSSLDSDD-----VFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 380420360 1011 MTQQQENLKFLSHF 1024
Cdd:cd11280    75 IRQGQEPREFWSLF 88
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-308 7.14e-19

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 86.76  E-value: 7.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  103 LDDLSVLDLSHNQLTEIPrDLENSRNMLVLNLSHNSIDNIPNqlFINLTDLLYLDLSDNNLDSLPPqMRRLVHLQTLILN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  183 NNPLMH-AQLRQLPvmvSLQTLHLRNtQRTQNNM-----PTSLEGLSN-LTDVDLSCNDLTRVpECLYSLVNLKRLNLSS 255
Cdd:cd21340    77 GNRISVvEGLENLT---NLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 380420360  256 NQIS---ELSLCIDQWTKLETLNLSRNqltslPsaICKLSKLK-KLYVNSNKID-FDG 308
Cdd:cd21340   152 NQISdleELLDLLSSWPSLRELDLTGN-----P--VCKKPKYRdKIILASKSLEvLDG 202
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-706 2.71e-18

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 80.74  E-value: 2.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  617 PTRLYRVYGKKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKNERKSKAEITTL--MQ 694
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLdeGD 80

                          90
                  ....*....|..
gi 380420360  695 NQEPPEFWEVLG 706
Cdd:cd11289    81 TNESPEFWKVLG 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 758-837 8.23e-18

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 79.64  E-value: 8.23e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    758 VVPELRLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALKLGQEVCGMLHrPKHAVVIRNLEGTECQVFKSKFKNW 837
Cdd:smart00262   12 RVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 500-593 5.87e-17

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 77.31  E-value: 5.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  500 VSVWQIENFIPIQVDEAFHGKFYEADCYIILKTFlDENGALNWQIFYWIGQDATLDKKAGAAIHAVNLRNYLGAECRTIR 579
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 380420360  580 EEMGDESEEFTVVF 593
Cdd:cd11293    88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 501-593 9.39e-17

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 76.56  E-value: 9.39e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    501 SVWQIENFIPIQVDE--AFHGKFYEADCYIILKTfldengalnWQIFYWIGQDATLDKKAGAAIHAVNLRNYLGAECRTI 578
Cdd:smart00262    1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                            90
                    ....*....|....*.
gi 380420360    579 RE-EMGDESEEFTVVF 593
Cdd:smart00262   72 RVvDEGKEPPEFWSLF 87
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
149-374 2.01e-16

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 83.06  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  149 NLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLILNNNPLMHAQLRQLPVMVSLQTLHLRNTQRTQNNMPTSLEGLSNLTDV 228
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  229 DLSCNDLTrvPECLYSLVNLKRLNLSSNQIselslcIDQWTKLETLNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDFdg 308
Cdd:COG4886    81 LLSLLLLG--LTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD-- 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380420360  309 LPSGVGKLSNLvefmaannnlelvpeglcrcgklKKLVLNKNRLVTLPEAIHFLTELEVLDVRENP 374
Cdd:COG4886   151 LPEPLGNLTNL-----------------------KSLDLSNNQLTDLPEELGNLTNLKELDLSNNQ 193
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
26-288 3.00e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 84.36  E-value: 3.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   26 PEHVKSMTSLR-WLKLNRTGLC-----------YLPEELASL--QKLEHLSVSHNslttLHGelsslpNLRAVVARANNL 91
Cdd:PRK15370  163 ANREEAVQRMRdCLKNNKTELRlkilglttipaCIPEQITTLilDNNELKSLPEN----LQG------NIKTLYANSNQL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   92 knSGVPDDIfqLDDLSVLDLSHNQLTEIPRDLENSrnMLVLNLSHNSIDNIPNqlfiNLTD-LLYLDLSDNNLDSLPPQM 170
Cdd:PRK15370  233 --TSIPATL--PDTIQEMELSINRITELPERLPSA--LQSLDLFHNKISCLPE----NLPEeLRYLSVYDNSIRTLPAHL 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  171 -RRLVHLqtLILNNNplmhaqLRQLPVMVSLQTLHLRNTQRTQNNMPTSLEglSNLTDVDLSCNDLTRVPECLYSlvNLK 249
Cdd:PRK15370  303 pSGITHL--NVQSNS------LTALPETLPPGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLPP--TIT 370

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 380420360  250 RLNLSSNQISELSLCIDqwTKLETLNLSRNQLTSLPSAI 288
Cdd:PRK15370  371 TLDVSRNALTNLPENLP--AALQIMQASRNNLVRLPESL 407
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1047-1139 1.09e-14

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 70.78  E-value: 1.09e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   1047 YHIRTNGSaLCTRTIQIATDSSNLNSEFCFILkvpfestDNQGIVYTWVGRAADPDE----AKLAEEIMNTMFDDTYSKQ 1122
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEkkkaAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 380420360   1123 VINEGEEPENFFWVGIG 1139
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
627-702 1.58e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.64  E-value: 1.58e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380420360   627 KNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKNERKSKAEITTLMQNQEPPEFW 702
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-707 1.74e-14

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 69.95  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  617 PTRLYRVYG--KKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGgnatLGGTTKARLFAEKINKNeRKSKAEITTLMQ 694
Cdd:cd11288     2 PTRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVG----KGSSEDERELAKDVASF-LKPKASLQEVAE 76

                          90
                  ....*....|...
gi 380420360  695 NQEPPEFWEVLGG 707
Cdd:cd11288    77 GSEPDEFWEALGG 89
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
165-450 1.81e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.12  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  165 SLPPQmrrlvhLQTLILNNNplmhaQLRQLP--VMVSLQTLHLRNTQRTQnnMPTSLEglSNLTDVDLSCNDLTRVPECL 242
Cdd:PRK15370  196 CIPEQ------ITTLILDNN-----ELKSLPenLQGNIKTLYANSNQLTS--IPATLP--DTIQEMELSINRITELPERL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  243 YSLvnLKRLNLSSNQISELSLCIDQwtKLETLNLSRNQLTSLPSAICklSKLKKLYVNSNKIDFdgLPSGVGklSNLVEF 322
Cdd:PRK15370  261 PSA--LQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLP--SGITHLNVQSNSLTA--LPETLP--PGLKTL 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  323 MAANNNLELVPEGLCRcgKLKKLVLNKNRLVTLPEAIHflTELEVLDVRENPNLVMP---PKPVDRTAEWYNIDFSLQNQ 399
Cdd:PRK15370  331 EAGENALTSLPASLPP--ELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPenlPAALQIMQASRNNLVRLPES 406

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 380420360  400 L---RLAGASPATVAAAGGGNSPR--DHMARKMrlrrckdSAHDDQAKQVLKGMSD 450
Cdd:PRK15370  407 LphfRGEGPQPTRIIVEYNPFSERtiQNMQRLM-------SSVGYQGPRVLFAMGD 455
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
191-379 5.98e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.58  E-value: 5.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  191 LRQLPVMVSLQTLHLRNTQRTQNNMPTSLEGlsNLTDVDLSCNDLTRVPECLYSLVNLkrLNLSSNQISELSLCIDqwTK 270
Cdd:PRK15370  190 LTTIPACIPEQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPATLPDTIQE--MELSINRITELPERLP--SA 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  271 LETLNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDFDGLPSGVgklsnlVEFMAANNNLELVPEGLCRcgKLKKLVLNKN 350
Cdd:PRK15370  264 LQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGI------THLNVQSNSLTALPETLPP--GLKTLEAGEN 335

                         170       180
                  ....*....|....*....|....*....
gi 380420360  351 RLVTLPEAIHflTELEVLDVRENPNLVMP 379
Cdd:PRK15370  336 ALTSLPASLP--PELQVLDVSKNQITVLP 362
Gelsolin pfam00626
Gelsolin repeat;
507-589 6.45e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 65.02  E-value: 6.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   507 NFIPIQVDEAFHGKFYEADCYIILKTFldengalnwQIFYWIGQDATLDKKAGAAIHAVNLR-NYLGAECRTIREEMGDE 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....
gi 380420360   586 SEEF 589
Cdd:pfam00626   72 PARF 75
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 199-369 9.87e-13

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 68.66  E-value: 9.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  199 SLQTLHLRNtqrtqNNMpTSLEGLS---NLTDVDLSCNDLTRVpECLYSLVNLKRLNLSSNQISELS-LciDQWTKLETL 274
Cdd:cd21340    25 NLKVLYLYD-----NKI-TKIENLEfltNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISVVEgL--ENLTNLEEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  275 NLSRNQL------TSLPSAICKLSK-LKKLYVNSNKIDFdglPSGVGKLSNLVEFMAANNNL----ELVPEgLCRCGKLK 343
Cdd:cd21340    96 HIENQRLppgeklTFDPRSLAALSNsLRVLNISGNNIDS---LEPLAPLRNLEQLDASNNQIsdleELLDL-LSSWPSLR 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 380420360  344 KLVLNKNRLVTLP----EAIHFLTELEVLD 369
Cdd:cd21340   172 ELDLTGNPVCKKPkyrdKIILASKSLEVLD 201
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 91-374 6.41e-12

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 68.15  E-value: 6.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   91 LKNSGVPDDIFQLDDLSVLDLSHNQLTE-----IPRDLENSRNMLVLNLSHNSIDNIPNQL------FINLTDLLYLDLS 159
Cdd:cd00116    10 LKTERATELLPKLLCLQVLRLEGNTLGEeaakaLASALRPQPSLKELCLSLNETGRIPRGLqsllqgLTKGCGLQELDLS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  160 DNNL-DSLPPQMRRLVH---LQTLILNNNPLMHAQLRQLPVMVSLQTLHLRNTQRTQNNM-PTSLEGLSN-------LTD 227
Cdd:cd00116    90 DNALgPDGCGVLESLLRsssLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLeGASCEALAKalranrdLKE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  228 VDLSCNDL-----TRVPECLYSLVNLKRLNLSSNQI-----SELSLCIDQWTKLETLNLSRNQLTSLP-SAICK-----L 291
Cdd:cd00116   170 LNLANNGIgdagiRALAEGLKANCNLEVLDLNNNGLtdegaSALAETLASLKSLEVLNLGDNNLTDAGaAALASallspN 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  292 SKLKKLYVNSNKIDFDGLPSgvgklsnLVEFMAANNNlelvpeglcrcgkLKKLVLNKNRLVTLPEAIHFLT------EL 365
Cdd:cd00116   250 ISLLTLSLSCNDITDDGAKD-------LAEVLAEKES-------------LLELDLRGNKFGEEGAQLLAESllepgnEL 309


                  ....*....
gi 380420360  366 EVLDVRENP 374
Cdd:cd00116   310 ESLWVKDDS 318
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
131-374 1.30e-11

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 69.04  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  131 VLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQMRRL--------------VHLQTLILNNNPLMHaqlrqLPV 196
Cdd:PRK15387  205 VLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELRTLevsgnqltslpvlpPGLLELSIFSNPLTH-----LPA 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  197 MVS-LQTLHLRNTQRTqnNMPTSLEGLSNLTdvdLSCNDLTRVPECLYSLVNLKRLNlssNQISELSLCIdqwTKLETLN 275
Cdd:PRK15387  280 LPSgLCKLWIFGNQLT--SLPVLPPGLQELS---VSDNQLASLPALPSELCKLWAYN---NQLTSLPTLP---SGLQELS 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  276 LSRNQLTSLPSAIcklSKLKKLYVNSNKI-DFDGLPSGVGKL--------------SNLVEFMAANN---NLELVPEGLC 337
Cdd:PRK15387  349 VSDNQLASLPTLP---SELYKLWAYNNRLtSLPALPSGLKELivsgnrltslpvlpSELKELMVSGNrltSLPMLPSGLL 425

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 380420360  338 rcgklkKLVLNKNRLVTLPEAIHFLTELEVLDVRENP 374
Cdd:PRK15387  426 ------SLSVYRNQLTRLPESLIHLSSETTVNLEGNP 456
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1155-1254 2.47e-11

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 60.84  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1155 RLFRCSNEK-GYFAVSEKCSDfcqdDLADDDIMLLDNGKEVYMWVGTQTSQVEiklsLKACQVYIQHMRSKDTENPRKLR 1233
Cdd:cd11280     3 RLYRVRGSKaIEIEEVPLASS----SLDSDDVFVLDTGSEIYIWQGRASSQAE----LAAAALLAKELDEERKGKPEIVR 74

                          90       100
                  ....*....|....*....|.
gi 380420360 1234 lVRKGNEPHCFtrcfhaWSAF 1254
Cdd:cd11280    75 -IRQGQEPREF------WSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 618-701 3.05e-11

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 61.11  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  618 TRLYRVY---GKKNIRL-ESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEK-INKNERKSKAEITTL 692
Cdd:cd11292     4 KKLYKVSdasGKLKLTEvAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEfLRKKKRPPYTQVTRV 83


                  ....*....
gi 380420360  693 MQNQEPPEF 701
Cdd:cd11292    84 TEGGESALF 92
LRR_8 pfam13855
Leucine rich repeat;
127-186 3.87e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 3.87e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380420360   127 RNMLVLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQM-RRLVHLQTLILNNNPL 186
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 50-188 9.30e-11

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.88  E-value: 9.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   50 EELASLQKLEHLSVSHNSLTTLHGeLSSLPNLR---------AVVaraNNLKNsgvpddifqLDDLSVLDLSHNQLTE-- 118
Cdd:cd21340    40 ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKklylggnriSVV---EGLEN---------LTNLEELHIENQRLPPge 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380420360  119 ----IPRDLENSRNML-VLNLSHNSIDNIpNQLFiNLTDLLYLDLSDNNLDSLPPQ---MRRLVHLQTLILNNNPLMH 188
Cdd:cd21340   107 kltfDPRSLAALSNSLrVLNISGNNIDSL-EPLA-PLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCK 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-225 5.46e-10

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 5.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    7 LPFIRGVDLSGNDFKggNFPEHVKSMTSLRWLKLNRTGLCYLPEELASLQKLEHLSVSHNSLTTLHG------------- 73
Cdd:COG4886   181 LTNLKELDLSNNQIT--DLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPElgnltnleeldls 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   74 --------ELSSLPNLRAVVARANNLKNsgvpddiFQLDDLSVLDLSHNQLTEIPRDLENSRNMLVLNLSHNSIDNIPNQ 145
Cdd:COG4886   259 nnqltdlpPLANLTNLKTLDLSNNQLTD-------LKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLK 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  146 LFINLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLILNNNPLMHAQLRQLPVMVSLQTLHLRNTQRTQNNMPTSLEGLSNL 225
Cdd:COG4886   332 GLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 222-373 2.12e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 59.03  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  222 LSNLTDVDLSCNDLTRVPEcLYSLVNLKRLNLSSNQISELSlCIDQWTKLETLNLSRNQLTSLPSaICKLSKLKKLYVNS 301
Cdd:cd21340     1 LKRITHLYLNDKNITKIDN-LSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  302 NKIdfdGLPSGVGKLSNLVEFMAANNNLELvPEGLC---RC-----GKLKKLVLNKNRLVTLpEAIHFLTELEVLDVREN 373
Cdd:cd21340    78 NRI---SVVEGLENLTNLEELHIENQRLPP-GEKLTfdpRSlaalsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152
LRR_8 pfam13855
Leucine rich repeat;
223-281 9.71e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.53  E-value: 9.71e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380420360   223 SNLTDVDLSCNDLTRV-PECLYSLVNLKRLNLSSNQISELSL-CIDQWTKLETLNLSRNQL 281
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 502-593 1.31e-08

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 53.14  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  502 VWQIENFIPIQVDE--AFHGKFYEADCYIiLKTFLdengalnwQIFYWIGQDATLDKKAGAAIHAVNLRNYLGAECRTIR 579
Cdd:cd11280     4 LYRVRGSKAIEIEEvpLASSSLDSDDVFV-LDTGS--------EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 380420360  580 EEMGDESEEFTVVF 593
Cdd:cd11280    75 IRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1154-1248 1.34e-08

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 53.41  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1154 ARLFRCSNEKGYFAVSE-KCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHM-RSKDTenprK 1231
Cdd:cd11292     4 KKLYKVSDASGKLKLTEvAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKkRPPYT----Q 79

                          90
                  ....*....|....*..
gi 380420360 1232 LRLVRKGNEPHCFTRCF 1248
Cdd:cd11292    80 VTRVTEGGESALFKSKF 96
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
38-325 1.89e-08

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 59.02  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   38 LKLNRTGLCYLPEELASlqKLEHLSVSHNSLTTLHgelSSLPNLRAVVARANNLKNSGV-PDDIFQLDDLSvldlshNQL 116
Cdd:PRK15387  206 LNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLP---ALPPELRTLEVSGNQLTSLPVlPPGLLELSIFS------NPL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  117 TEIPRDLENSRNMLVLNLSHNSIDNIPnqlfinlTDLLYLDLSDNNLDSLPPQMRRLVHLQTLilnNNplmhaQLRQLPV 196
Cdd:PRK15387  275 THLPALPSGLCKLWIFGNQLTSLPVLP-------PGLQELSVSDNQLASLPALPSELCKLWAY---NN-----QLTSLPT 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  197 MVS-LQTLHLRNTQRTQ--------------NNMPTSLEGL-SNLTDVDLSCNDLTRVPeCLYSlvNLKRLNLSSNQISE 260
Cdd:PRK15387  340 LPSgLQELSVSDNQLASlptlpselyklwayNNRLTSLPALpSGLKELIVSGNRLTSLP-VLPS--ELKELMVSGNRLTS 416

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380420360  261 LSLCIdqwTKLETLNLSRNQLTSLPSAICKLSklkklyvNSNKIDFDGLPSGVGKLSNLVEFMAA 325
Cdd:PRK15387  417 LPMLP---SGLLSLSVYRNQLTRLPESLIHLS-------SETTVNLEGNPLSERTLQALREITSA 471
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 769-838 2.15e-08

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 53.07  E-value: 2.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380420360  769 LDTKGVYILDCWSDVFIWIGRKSPRLVRAAALKLGQ---EVCGMLHRPKHAVVIRNLEGTECQVFKSKFKNWD 838
Cdd:cd11291    27 LDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkyiETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1043-1135 4.15e-08

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 51.98  E-value: 4.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1043 QPSLYHIRTNGSalcTRTIQIATDSSNLNSEFCFILkvpfestDNQGIVYTWVGRAADPDE----AKLAEEIMNTMFDDT 1118
Cdd:cd11280     1 PPRLYRVRGSKA---IEIEEVPLASSSLDSDDVFVL-------DTGSEIYIWQGRASSQAElaaaALLAKELDEERKGKP 70

                          90
                  ....*....|....*..
gi 380420360 1119 YSkQVINEGEEPEnFFW 1135
Cdd:cd11280    71 EI-VRIRQGQEPR-EFW 85
Gelsolin pfam00626
Gelsolin repeat;
755-831 8.36e-08

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 50.77  E-value: 8.36e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380420360   755 KLDVVPELRLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALKLGQEVcGMLHRPKHAVVIRNLEGTECQVFK 831
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1041-1133 1.17e-07

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 50.71  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1041 SVQPSLYHIRTNGSALctRTIQIATDSSN---LNSEFCFILkvpfestDNQGIVYTWVGRAADPDEAK----LAEEIMNT 1113
Cdd:cd11292     1 AEQKKLYKVSDASGKL--KLTEVAEGSLNqemLDSEDCYIL-------DCGSEIFVWVGKGASLDERKaalkNAEEFLRK 71

                          90       100
                  ....*....|....*....|.
gi 380420360 1114 MFDDTYSK-QVINEGEEPENF 1133
Cdd:cd11292    72 KKRPPYTQvTRVTEGGESALF 92
LRR_8 pfam13855
Leucine rich repeat;
247-304 1.30e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.45  E-value: 1.30e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380420360   247 NLKRLNLSSNQISELSlciDQW----TKLETLNLSRNQLTSL-PSAICKLSKLKKLYVNSNKI 304
Cdd:pfam13855    2 NLRSLDLSNNRLTSLD---DGAfkglSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 10-163 2.22e-07

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 54.28  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   10 IRGVDLSGNDFKGGNFP--EHVKSMTSLRWLKLNR------------TGLCYLPEELASLQkLEHLSVSHNSLTTLHGEL 75
Cdd:cd00116    83 LQELDLSDNALGPDGCGvlESLLRSSSLQELKLNNnglgdrglrllaKGLKDLPPALEKLV-LGRNRLEGASCEALAKAL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   76 SSLPNLRAVVARANNLKNSGVP---DDIFQLDDLSVLDLSHNQLT--------EIPRDLensRNMLVLNLSHNSIDNIP- 143
Cdd:cd00116   162 RANRDLKELNLANNGIGDAGIRalaEGLKANCNLEVLDLNNNGLTdegasalaETLASL---KSLEVLNLGDNNLTDAGa 238

                         170       180
                  ....*....|....*....|....
gi 380420360  144 ----NQLFINLTDLLYLDLSDNNL 163
Cdd:cd00116   239 aalaSALLSPNISLLTLSLSCNDI 262
Gelsolin pfam00626
Gelsolin repeat;
1166-1227 4.87e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.46  E-value: 4.87e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380420360  1166 FAVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTE 1227
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPE 62
LRR_8 pfam13855
Leucine rich repeat;
199-258 1.08e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.75  E-value: 1.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380420360   199 SLQTLHLRNTqRTQNNMPTSLEGLSNLTDVDLSCNDLTRV-PECLYSLVNLKRLNLSSNQI 258
Cdd:pfam13855    2 NLRSLDLSNN-RLTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 641-701 3.41e-06

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 46.91  E-value: 3.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380420360  641 LDPQFVFLLDTGLEIYVWRGGNAT----LGGTTKARLFAEKINKNERKSKAEITTLMQNQEPPEF 701
Cdd:cd11291    27 LDTDDIMLLDTGDEVFVWVGSESSdeekKEALTSAKKYIETDPLGRSKPRTPIYLVKQGNEPPTF 91
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
25-263 4.80e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.93  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   25 FPEHVksmTSLRWLKLNRTGLCYLPEELASLQklehlsVSHNSLTTL-------------HGELSSLPNLRAVVARANNL 91
Cdd:PRK15387  220 LPAHI---TTLVIPDNNLTSLPALPPELRTLE------VSGNQLTSLpvlppgllelsifSNPLTHLPALPSGLCKLWIF 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   92 KN--SGVPDDIFQLDDLSVLDlshNQLTEIPRDLENSRNMLVLNLSHNSIDNIPnqlfinlTDLLYLDLSDNNLDSLPPQ 169
Cdd:PRK15387  291 GNqlTSLPVLPPGLQELSVSD---NQLASLPALPSELCKLWAYNNQLTSLPTLP-------SGLQELSVSDNQLASLPTL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  170 MRRLVHLQTL--ILNNNPLMHAQLRQLPV----MVSLQTL--HLRNTQRTQNNMpTSLEGL-SNLTDVDLSCNDLTRVPE 240
Cdd:PRK15387  361 PSELYKLWAYnnRLTSLPALPSGLKELIVsgnrLTSLPVLpsELKELMVSGNRL-TSLPMLpSGLLSLSVYRNQLTRLPE 439

                         250       260
                  ....*....|....*....|...
gi 380420360  241 CLYSLVNLKRLNLSSNQISELSL 263
Cdd:PRK15387  440 SLIHLSSETTVNLEGNPLSERTL 462
LRR_8 pfam13855
Leucine rich repeat;
79-139 5.19e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.82  E-value: 5.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380420360    79 PNLRAVVARANNLknSGVPDDIFQ-LDDLSVLDLSHNQLTEI-PRDLENSRNMLVLNLSHNSI 139
Cdd:pfam13855    1 PNLRSLDLSNNRL--TSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 75-298 6.46e-06

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 50.17  E-value: 6.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   75 LSSLPNLRAVVARANNLKNSGVPDDIFQLDD---LSVLDLSHNQLT-----EIPRDLENSRNMLVLNLSHNSIDNIPNQL 146
Cdd:COG5238   204 LTQNTTVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQIGdegviALAEALKNNTTVETLYLSGNQIGAEGAIA 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  147 FINL----TDLLYLDLSDNNLDSlppqmRRLVHLQTLILNNNPlmhaqlrqlpvmvsLQTLHLRNTQRTQNNM---PTSL 219
Cdd:COG5238   284 LAKAlqgnTTLTSLDLSVNRIGD-----EGAIALAEGLQGNKT--------------LHTLNLAYNGIGAQGAialAKAL 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  220 EGLSNLTDVDLSCNDLT-----RVPECLYSLVNLKRLNLSSNQISEL---SLcID--QWTKLETLNLSRNQLTSLPSA-- 287
Cdd:COG5238   345 QENTTLHSLDLSDNQIGdegaiALAKYLEGNTTLRELNLGKNNIGKQgaeAL-IDalQTNRLHTLILDGNLIGAEAQQrl 423

                         250
                  ....*....|.
gi 380420360  288 ICKLSKLKKLY 298
Cdd:COG5238   424 EQLLERIKSVY 434
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 768-834 7.50e-06

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 45.44  E-value: 7.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380420360  768 LLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALKLgQEVCGMLHRPKhAVVIRNLEGTECQVFKSKF 834
Cdd:cd11280    24 SLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALL-AKELDEERKGK-PEIVRIRQGQEPREFWSLF 88
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 2-139 1.79e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 48.12  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360    2 AATGVLPFIRG---VDLSGNDFKGGNFP---EHVKSMTSLRWLKLNRTGLC-----YLPEELASLQKLEHLSVSHNSLT- 69
Cdd:cd00116   156 ALAKALRANRDlkeLNLANNGIGDAGIRalaEGLKANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTd 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   70 ----TLH-GELSSLPNLRAVVARANNLKNSGVPD---DIFQLDDLSVLDLSHNQLTEIPRDL------ENSRNMLVLNLS 135
Cdd:cd00116   236 agaaALAsALLSPNISLLTLSLSCNDITDDGAKDlaeVLAEKESLLELDLRGNKFGEEGAQLlaesllEPGNELESLWVK 315


                  ....
gi 380420360  136 HNSI 139
Cdd:cd00116   316 DDSF 319
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 917-1024 2.85e-05

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 44.18  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  917 ARLPEEEFGHFHTQDCYVFLCRYwvpveyeddkekgkekgeegddeekQPEEDFQCVVYFWQGREASnMGWLTFTFSLQK 996
Cdd:cd11293    20 VPVPKEEYGQFYGGDCYIVLYTY-------------------------QGGGKEEHILYFWQGRHSS-QDERAAAALLTV 73

                          90       100
                  ....*....|....*....|....*...
gi 380420360  997 KFESLFPGKLEVVRMTQQQENLKFLSHF 1024
Cdd:cd11293    74 ELDEELKGRAVQVRVVQGKEPPHFLALF 101
PLN03150 PLN03150
hypothetical protein; Provisional
 90-185 3.69e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 47.89  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   90 NLKNSG----VPDDIFQLDDLSVLDLSHNQLT-EIPRDLENSRNMLVLNLSHNSID-NIPNQLFiNLTDLLYLDLSDNNL 163
Cdd:PLN03150  424 GLDNQGlrgfIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLG-QLTSLRILNLNGNSL 502

                          90       100
                  ....*....|....*....|....
gi 380420360  164 DSLPPQM--RRLVHLQTLILNNNP 185
Cdd:PLN03150  503 SGRVPAAlgGRLLHRASFNFTDNA 526
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 224-401 9.16e-05

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 47.18  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  224 NLTDVDLSCNDLTRVPECLYSLVNLKRLNL--SSN--QISELSLCidqwTKLETLNLSR-NQLTSLPSAICKLSKLKKLY 298
Cdd:PLN03210  612 NLVKLQMQGSKLEKLWDGVHSLTGLRNIDLrgSKNlkEIPDLSMA----TNLETLKLSDcSSLVELPSSIQYLNKLEDLD 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  299 VnSNKIDFDGLPSGVGKLS----NL-------------------------VEFMAANNNLE-LVPEGLCRCGK------- 341
Cdd:PLN03210  688 M-SRCENLEILPTGINLKSlyrlNLsgcsrlksfpdistniswldldetaIEEFPSNLRLEnLDELILCEMKSeklwerv 766

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380420360  342 -------------LKKLVLNKN-RLVTLPEAIHFLTELEVLDVRENPNLVMPPKPVDRTAeWYNIDFSLQNQLR 401
Cdd:PLN03210  767 qpltplmtmlspsLTRLFLSDIpSLVELPSSIQNLHKLEHLEIENCINLETLPTGINLES-LESLDLSGCSRLR 839
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 269-311 1.23e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 40.69  E-value: 1.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 380420360   269 TKLETLNLSRNQLTSLPsAICKLSKLKKLYVNSNKI--DFDGLPS 311
Cdd:pfam12799    1 PNLEVLDLSNNQITDIP-PLAKLPNLETLDLSGNNKitDLSDLAN 44
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 247-285 1.39e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 40.31  E-value: 1.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 380420360   247 NLKRLNLSSNQISELSLcIDQWTKLETLNLSRN-QLTSLP 285
Cdd:pfam12799    2 NLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLS 40
Gelsolin pfam00626
Gelsolin repeat;
1066-1133 1.50e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 41.52  E-value: 1.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380420360  1066 DSSNLNSEFCFILkvpfestDNQGIVYTWVGRAADPDE----AKLAEEIMNTMFDDTYSKQVINEGEEPENF 1133
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
PLN03150 PLN03150
hypothetical protein; Provisional
 119-186 1.60e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 45.96  E-value: 1.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  119 IPRDLENSRNMLVLNLSHNSID-NIPNQLFiNLTDLLYLDLSDNNLD-SLPPQMRRLVHLQTLILNNNPL 186
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIRgNIPPSLG-SITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSL 502
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 230-373 1.73e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.99  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  230 LSCNDLTRVpeclyslvnlKRLNLSSNQIS-ELSLCIDQWTKLETLNLSRNQLT-SLPSAICKLSKlKKLYVNSNKIDFD 307
Cdd:PLN00113   63 ITCNNSSRV----------VSIDLSGKNISgKISSAIFRLPYIQTINLSNNQLSgPIPDDIFTTSS-SLRYLNLSNNNFT 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380420360  308 GlPSGVGKLSNLVEFMAANNNLE-LVPEGLCRCGKLKKLVLNKNRLV-TLPEAIHFLTELEVLDVREN 373
Cdd:PLN00113  132 G-SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASN 198
LRR_8 pfam13855
Leucine rich repeat;
33-91 1.97e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.59  E-value: 1.97e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380420360    33 TSLRWLKLNRTGLCYLPEE-LASLQKLEHLSVSHNSLTTLH-GELSSLPNLRAVVARANNL 91
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 156-259 4.90e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.42  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  156 LDLSDNNLDS-LPPQMRRLVHLQTLILNNNPLmhaqlrqlpvmvslqtlhlrntqrtQNNMPTSLEGLSNLTDVDLSCND 234
Cdd:PLN03150  423 LGLDNQGLRGfIPNDISKLRHLQSINLSGNSI-------------------------RGNIPPSLGSITSLEVLDLSYNS 477

                          90       100
                  ....*....|....*....|....*.
gi 380420360  235 LT-RVPECLYSLVNLKRLNLSSNQIS 259
Cdd:PLN03150  478 FNgSIPESLGQLTSLRILNLNGNSLS 503
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 35-300 4.93e-04

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 44.48  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   35 LRWLKLNRTGLCYLP-----EELASLQ----KLEHLSVSHNSLT-----TLHGE--LSSLPNLravvARANNLKNSGV-- 96
Cdd:PLN03210  591 LRLLRWDKYPLRCMPsnfrpENLVKLQmqgsKLEKLWDGVHSLTglrniDLRGSknLKEIPDL----SMATNLETLKLsd 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   97 -------PDDIFQLDDLSVLDLSH-NQLTEIPRDLeNSRNMLVLNLSHNSIDNIpnqlFINL-TDLLYLDLSDNNLDSLP 167
Cdd:PLN03210  667 csslvelPSSIQYLNKLEDLDMSRcENLEILPTGI-NLKSLYRLNLSGCSRLKS----FPDIsTNISWLDLDETAIEEFP 741

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  168 PQMRrLVHLQTLIL----NNNPLMHAQLRQlPVMV----SLQTLHLRNTQrTQNNMPTSLEGLSNLTDVDL-SCNDLTRV 238
Cdd:PLN03210  742 SNLR-LENLDELILcemkSEKLWERVQPLT-PLMTmlspSLTRLFLSDIP-SLVELPSSIQNLHKLEHLEIeNCINLETL 818

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380420360  239 PECLySLVNLKRLNLSSnqISELSLCIDQWTKLETLNLSRNQLTSLPSAICKLSKLKKLYVN 300
Cdd:PLN03210  819 PTGI-NLESLESLDLSG--CSRLRTFPDISTNISDLNLSRTGIEEVPWWIEKFSNLSFLDMN 877
PLN03150 PLN03150
hypothetical protein; Provisional
 238-314 5.66e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.04  E-value: 5.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380420360  238 VPECLYSLVNLKRLNLSSNQI-SELSLCIDQWTKLETLNLSRNQLT-SLPSAICKLSKLKKLYVNSNKIDfDGLPSGVG 314
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLS-GRVPAALG 511
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 269-376 9.36e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 42.08  E-value: 9.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  269 TKLETLNLSRNQLTSLPS-AICKlsKLKKLYVNSNKID-FDGLPSgvgkLSNLVEFMAANNNLELVpEGLCRCGKLKKLV 346
Cdd:cd21340     2 KRITHLYLNDKNITKIDNlSLCK--NLKVLYLYDNKITkIENLEF----LTNLTHLYLQNNQIEKI-ENLENLVNLKKLY 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 380420360  347 LNKNRLVTLpEAIHFLTELEVLDVrENPNL 376
Cdd:cd21340    75 LGGNRISVV-EGLENLTNLEELHI-ENQRL 102
LRR_8 pfam13855
Leucine rich repeat;
269-311 1.41e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.27  E-value: 1.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 380420360   269 TKLETLNLSRNQLTSL-PSAICKLSKLKKLYVNSNKID------FDGLPS 311
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTtlspgaFSGLPS 50
PLN03150 PLN03150
hypothetical protein; Provisional
 33-139 4.85e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.95  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   33 TSLRW----LKLNRTGL-CYLPEELASLQKLEHLSVSHNSLttlHGElsslpnlravvarannlknsgVPDDIFQLDDLS 107
Cdd:PLN03150  414 TKGKWfidgLGLDNQGLrGFIPNDISKLRHLQSINLSGNSI---RGN---------------------IPPSLGSITSLE 469

                          90       100       110
                  ....*....|....*....|....*....|...
gi 380420360  108 VLDLSHNQLT-EIPRDLENSRNMLVLNLSHNSI 139
Cdd:PLN03150  470 VLDLSYNSFNgSIPESLGQLTSLRILNLNGNSL 502
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 64-373 6.79e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 40.54  E-value: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360   64 SHNSLTTLHGELSSlpNLRAVVARANNLKNSGVPD---------DIFQLDDLSVLDLSHNQLTEIPRDLENSRNMLVLNL 134
Cdd:COG5238    17 SANPATTEQSELTK--RATIVNLRSYHLHGGAILLarylqsrssITQYLRFEGQGDPGLNPVALEKAAEAFPTQLLVVDW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  135 SHNSIDNI---PNQLFINLT--DLLYLDLSDNNLDSLPPqmrRLVHLQTLILnnnplmHAQLRQLPVMVS-LQTLHLRNT 208
Cdd:COG5238    95 EGAEEVSPvalAETATAVATppPDLRRIMAKTLEDSLIL---YLALPRRINL------IQVLKDPLGGNAvHLLGLAARL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  209 QRTQNNMPTSLEGLSNLTDVDLSCNdltrvpeclyslvnlkrlNLSSNQISELSLCIDQWTKLETLNLSRNQLT-----S 283
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLGCN------------------QIGDEGIEELAEALTQNTTVTTLWLKRNPIGdegaeI 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360  284 LPSAICKLSKLKKLYVNSNKIDFDGlpsgvgkLSNLVEFMAANNNLE---------------LVPEGLCRCGKLKKLVLN 348
Cdd:COG5238   228 LAEALKGNKSLTTLDLSNNQIGDEG-------VIALAEALKNNTTVEtlylsgnqigaegaiALAKALQGNTTLTSLDLS 300

                         330       340       350
                  ....*....|....*....|....*....|
gi 380420360  349 KNRL-----VTLPEAIHFLTELEVLDVREN 373
Cdd:COG5238   301 VNRIgdegaIALAEGLQGNKTLHTLNLAYN 330
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 224-262 7.09e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 35.68  E-value: 7.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 380420360   224 NLTDVDLSCNDLTRVPEcLYSLVNLKRLNLSSN-QISELS 262
Cdd:pfam12799    2 NLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLS 40
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1154-1248 7.16e-03

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 37.22  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420360 1154 ARLFRCSNEKgyfAVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIklsLKACQvYIQHMRSKDTENPRKLR 1233
Cdd:cd11289     2 PRLLHVKGRR---NVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEK---AKAMQ-LAQGIRDERRLGRAKVI 74

                          90
                  ....*....|....*..
gi 380420360 1234 LVR--KGNEPHCFTRCF 1248
Cdd:cd11289    75 VLDegDTNESPEFWKVL 91
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 106-144 8.14e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 35.30  E-value: 8.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 380420360   106 LSVLDLSHNQLTEIPrDLENSRNMLVLNLSHN----SIDNIPN 144
Cdd:pfam12799    3 LEVLDLSNNQITDIP-PLAKLPNLETLDLSGNnkitDLSDLAN 44
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 131-163 9.53e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 35.30  E-value: 9.53e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 380420360   131 VLNLSHNSIDNIPNqlFINLTDLLYLDLSDNNL 163
Cdd:pfam12799    5 VLDLSNNQITDIPP--LAKLPNLETLDLSGNNK 35
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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